纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | E1A |
Uniprot No | Q9UPM8 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-1137aa |
氨基酸序列 | MSDIVEKTLTALPGLFLQNQPGGGPAAAKASFSSRLGSLVRGITALTSKHEEEKLIQQELSSLKATVSAPTTTLKMMKECMVRLIYCEMLGYDASFGYIHAIKLAQQGNLLEKRVGYLAVSLFLHESHELLLLLVNTVVKDLQSTNLVEVCMALTVVSQIFPCEMIPAVLPLIEDKLQHSKEIVRRKAVLALYKFHLIAPNQVQHIHIKFRKALCDRDVGVMAASLHIYLRMIKENSSGYKDLTGSFVTILKQVVGGKLPVEFNYHSVPAPWLQIQLLRILGLLGKDDQRTSELMYDVLDESLRRAELNHNVTYAILFECVHTVYSIYPKSELLEKAAKCIGKFVLSPKINLKYLGLKALTYVIQQDPTLALQHQMTIIECLDHPDPIIKRETLELLYRITNAQNITVIVQKMLEYLHQSKEEYVIVNLVGKIAELAEKYAPDNAWFIQTMNAVFSVGGDVMHPDIPNNFLRLLAEGFDDETEDQQLRLYAVQSYLTLLDMENVFYPQRFLQVMSWVLGEYSYLLDKETPEEVIAKLYKLLMNDSVSSETKAWLIAAVTKLTSQAHSSNTVERLIHEFTISLDTCMRQHAFELKHLHENVELMKSLLPVDRSCEDLVVDASLSFLDGFVAEGLSQGAAPYKPPHQRQEEKLSQEKVLNFEPYGLSFSSSGFTGRQSPAGISLGSDVSGNSAETGLKETNSLKLEGIKKLWGKEGYLPKKESKTGDESGALPVPQESIMENVDQAITKKDQSQVLTQSKEEKEKQLLASSLFVGLGSESTINLLGKADTVSHKFRRKSKVKEAKSGETTSTHNMTCSSFSSLSNVAYEDDYYSNTLHDTGDKELKKFSLTSELLDSESLTELPLVEKFSYCSLSTPSLFANNNMEIFHPPQSTAASVAKESSLASSFLEETTEYIHSNAMEVCNNETISVSSYKIWKDDCLLMVWSVTNKSGLELKSADLEIFPAENFKVTEQPGCCLPVMEAESTKSFQYSVQIEKPFTEGNLTGFISYHMMDTHSAQLEFSVNLSLLDFIRPLKISSDDFGKLWLSFANDVKQNVKMSESQAALPSALKTLQQKLRLHIIEIIGNEGLLACQLLPSIPCLLHCRVHADVLALWFRSSCSTLPDYLLYQCQKVMEGS |
预测分子量 | 127,2 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇关于E1A重组蛋白的经典文献摘要概括(基于真实研究领域,文献标题和作者为虚构示例,仅供参考):
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1. **文献名称**: *"Adenovirus E1A-mediated tumor suppression through interaction with p300/CBP"*
**作者**: Smith J. et al.
**摘要**: 研究揭示了腺病毒E1A重组蛋白通过结合宿主细胞中的p300/CBP共激活因子,抑制肿瘤细胞增殖的分子机制,为癌症治疗提供新靶点。
2. **文献名称**: *"E1A recombinant protein induces apoptosis in cancer cells via mitochondrial pathway"*
**作者**: Chen L. et al.
**摘要**: 实验证明E1A重组蛋白通过激活线粒体凋亡通路,选择性诱导多种癌细胞凋亡,但对正常细胞影响较小,提示其作为抗癌药物的潜力。
3. **文献名称**: *"Modulation of chromatin remodeling by E1A in gene therapy applications"*
**作者**: García-Rodríguez F. et al.
**摘要**: 该研究探讨了E1A重组蛋白通过调控染色质重塑复合物(如SWI/SNF)增强外源基因表达的效率,优化了腺病毒载体在基因治疗中的应用。
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**说明**:以上文献信息为领域相关方向的概括性示例,实际引用需查询真实数据库(如PubMed)获取具体文献。E1A蛋白研究多集中于肿瘤抑制、基因调控及病毒载体开发等领域。
The E1A recombinant protein originates from the early region 1A (E1A) of adenoviruses, primarily adenovirus type 5 (Ad5). E1A is a multifunctional regulatory protein critical for viral replication and host cell manipulation. In the viral life cycle, E1A acts as a master transcriptional regulator, hijacking cellular machinery to drive viral gene expression while modulating host cell processes like cell cycle progression, apoptosis, and immune responses. Its ability to interact with key cellular proteins, such as retinoblastoma (pRb) and p300/CBP transcriptional coactivators, enables it to dysregulate normal cell growth controls, promoting S-phase entry to create a replication-friendly environment.
In recombinant form, E1A has been engineered for research and therapeutic applications. Researchers leverage its properties to study oncogenesis, tumor suppression, and transcriptional regulation. Notably, E1A exhibits paradoxical roles: while it can immortalize cells by disrupting pRb-mediated growth inhibition, it also demonstrates tumor-suppressive activity in certain contexts. Studies highlight its potential in cancer therapy, particularly in suppressing metastasis and enhancing chemo/radiosensitivity by downregulating oncogenic pathways like HER2/neu. E1A’s ability to induce apoptosis in transformed cells has spurred interest in gene therapy strategies, though concerns about off-target effects on normal cells persist.
Recombinant E1A is typically produced in bacterial or eukaryotic expression systems, purified for functional studies. Its modular domains, including conserved regions (CR1-CR3) mediating protein interactions, are dissected to understand structure-function relationships. Despite promising preclinical results, clinical translation remains cautious due to risks of immune activation and potential toxicity. Ongoing research aims to optimize E1A-derived peptides or engineered variants for targeted anticancer therapies while minimizing adverse impacts.
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